메뉴 건너뛰기




Volumn 9, Issue 1, 2014, Pages

Correction: Identification of immunity-related genes in ostrinia furnacalis against entomopathogenic fungi by RNA-seq analysis (PLoS ONE (2014) 9, 1 (e86436) DOI: 10.1371/journal.pone.0086436);Identification of immunity-related genes in Ostrinia furnacalis against entomopathogenic fungi by RNA-seq analysis

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; CECROPIN; DEFENSIN; LYSOZYME; MYELOID DIFFERENTIATION FACTOR 88; NITRIC OXIDE SYNTHASE; PEPTIDOGLYCAN RECOGNITION PROTEIN; PEROXIDASE; PEROXIREDOXIN; PROTEIN INHIBITOR OF ACTIVATED STAT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SCAVENGER RECEPTOR; SERINE PROTEINASE INHIBITOR; STAT PROTEIN; SUPEROXIDE DISMUTASE; SUPPRESSOR OF CYTOKINE SIGNALING; THIOREDOXIN REDUCTASE; TRANSCRIPTOME; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2;

EID: 84898428911     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/annotation/755a38b9-ccc1-4042-baa2-1249c9da8670     Document Type: Erratum
Times cited : (68)

References (111)
  • 1
    • 33747595430 scopus 로고    scopus 로고
    • Host-pathogen interactions in drosophila: New tricks from an old friend
    • DOI 10.1038/ni1388, PII NI1388
    • Cherry S, Silverman N (2006) Host-pathogen interactions in drosophila: new tricks from an old friend. Nat Immunol 7: 911-917. (Pubitemid 44263904)
    • (2006) Nature Immunology , vol.7 , Issue.9 , pp. 911-917
    • Cherry, S.1    Silverman, N.2
  • 6
    • 34047268684 scopus 로고    scopus 로고
    • The host defense of Drosophila melanogaster
    • DOI 10.1146/annurev.immunol.25.022106.141615
    • Lemaitre B, Hoffmann J (2007) The host defense of Drosophila melanogaster. Annu Rev Immunol 25: 697-743. (Pubitemid 46697922)
    • (2007) Annual Review of Immunology , vol.25 , pp. 697-743
    • Lemaitre, B.1    Hoffmann, J.2
  • 7
    • 44649197623 scopus 로고    scopus 로고
    • The proPO-system: Pros and cons for its role in invertebrate immunity
    • Cerenius L, Lee BL, Soderhall K (2008) The proPO-system: pros and cons for its role in invertebrate immunity. Trends Immunol 29: 263-271.
    • (2008) Trends Immunol , vol.29 , pp. 263-271
    • Cerenius, L.1    Lee, B.L.2    Soderhall, K.3
  • 9
    • 0037013856 scopus 로고    scopus 로고
    • The Toll and Imd pathways are the major regulators of the immune response in Drosophila
    • DOI 10.1093/emboj/21.11.2568
    • De Gregorio E, Spellman PT, Tzou P, Rubin GM, Lemaitre B (2002) The Toll and Imd pathways are the major regulators of the immune response in Drosophila. The EMBO journal 21: 2568-2579. (Pubitemid 34619373)
    • (2002) EMBO Journal , vol.21 , Issue.11 , pp. 2568-2579
    • De Gregorio, E.1    Spellman, P.T.2    Tzou, P.3    Rubin, G.M.4    Lemaitre, B.5
  • 10
    • 33646037067 scopus 로고    scopus 로고
    • Drosophila immunity: A large-scale in vivo RNAi screen identifies five serine proteases required for Toll activation
    • Kambris Z, Brun S, Jang IH, Nam HJ, Romeo Y, et al. (2006) Drosophila immunity: a large-scale in vivo RNAi screen identifies five serine proteases required for Toll activation. CB 16: 808-813.
    • (2006) CB , vol.16 , pp. 808-813
    • Kambris, Z.1    Brun, S.2    Jang, I.H.3    Nam, H.J.4    Romeo, Y.5
  • 11
    • 35549006674 scopus 로고    scopus 로고
    • The Drosophila systemic immune response: Sensing and signalling during bacterial and fungal infections
    • DOI 10.1038/nri2194, PII NRI2194
    • Ferrandon D, Imler JL, Hetru C, Hoffmann JA (2007) The Drosophila systemic immune response: sensing and signalling during bacterial and fungal infections. Nat Rev Immunol 7: 862-874. (Pubitemid 350006241)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.11 , pp. 862-874
    • Ferrandon, D.1    Imler, J.-L.2    Hetru, C.3    Hoffmann, J.A.4
  • 12
    • 52549093726 scopus 로고    scopus 로고
    • Sensing of 'danger signals' and pathogen-associated molecular patterns defines binary signaling pathways 'upstream' of Toll
    • El Chamy L, Leclerc V, Caldelari I, Reichhart JM (2008) Sensing of 'danger signals' and pathogen-associated molecular patterns defines binary signaling pathways 'upstream' of Toll. Nat Immunol 9: 1165-1170.
    • (2008) Nat Immunol , vol.9 , pp. 1165-1170
    • El Chamy, L.1    Leclerc, V.2    Caldelari, I.3    Reichhart, J.M.4
  • 13
    • 33748795547 scopus 로고    scopus 로고
    • Two proteases defining a melanization cascade in the immune system of Drosophila
    • DOI 10.1074/jbc.M601642200
    • Tang H, Kambris Z, Lemaitre B, Hashimoto C (2006) Two proteases defining a melanization cascade in the immune system of Drosophila. J Biol Chem 281: 28097-28104. (Pubitemid 44414523)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.38 , pp. 28097-28104
    • Tang, H.1    Kambris, Z.2    Lemaitre, B.3    Hashimoto, C.4
  • 14
    • 84863281623 scopus 로고    scopus 로고
    • Genetic evidence of a redox-dependent systemic wound response via Hayan protease-phenoloxidase system in Drosophila
    • Nam HJ, Jang IH, You H, Lee KA, Lee WJ (2012) Genetic evidence of a redox-dependent systemic wound response via Hayan protease-phenoloxidase system in Drosophila. EMBO J 31: 1253-1265.
    • (2012) EMBO J , vol.31 , pp. 1253-1265
    • Nam, H.J.1    Jang, I.H.2    You, H.3    Lee, K.A.4    Lee, W.J.5
  • 15
    • 84877881327 scopus 로고    scopus 로고
    • Hemolymph Melanization in the Silkmoth Bombyx mori Involves Formation of a High Molecular Mass Complex That Metabolizes Tyrosine
    • Clark KD, Strand MR (2013) Hemolymph Melanization in the Silkmoth Bombyx mori Involves Formation of a High Molecular Mass Complex That Metabolizes Tyrosine. J Biol Chem 288: 14476-14487.
    • (2013) J Biol Chem , vol.288 , pp. 14476-14487
    • Clark, K.D.1    Strand, M.R.2
  • 16
    • 84859947791 scopus 로고    scopus 로고
    • Hindgut innate immunity and regulation of fecal microbiota through melanization in insects
    • Shao Q, Yang B, Xu Q, Li X, Lu Z, et al. (2012) Hindgut innate immunity and regulation of fecal microbiota through melanization in insects. J Biol Chem 287: 14270-14279.
    • (2012) J Biol Chem , vol.287 , pp. 14270-14279
    • Shao, Q.1    Yang, B.2    Xu, Q.3    Li, X.4    Lu, Z.5
  • 17
    • 67749097945 scopus 로고    scopus 로고
    • Functions of Manduca sexta hemolymph proteinases HP6 and HP8 in two innate immune pathways
    • An C, Ishibashi J, Ragan EJ, Jiang H, Kanost MR (2009) Functions of Manduca sexta hemolymph proteinases HP6 and HP8 in two innate immune pathways. J Biol Chem 284: 19716-19726.
    • (2009) J Biol Chem , vol.284 , pp. 19716-19726
    • An, C.1    Ishibashi, J.2    Ragan, E.J.3    Jiang, H.4    Kanost, M.R.5
  • 18
    • 34249707378 scopus 로고    scopus 로고
    • Manduca sexta hemolymph proteinase 21 activates prophenoloxidase- activating proteinase 3 in an insect innate immune response proteinase cascade
    • DOI 10.1074/jbc.M611243200
    • Gorman MJ, Wang Y, Jiang H, Kanost MR (2007) Manduca sexta hemolymph proteinase 21 activates prophenoloxidase-activating proteinase 3 in an insect innate immune response proteinase cascade. J Biol Chem 282: 11742-11749. (Pubitemid 47100681)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.16 , pp. 11742-11749
    • Gorman, M.J.1    Wang, Y.2    Jiang, H.3    Kanost, M.R.4
  • 19
    • 0037423271 scopus 로고    scopus 로고
    • Prophenoloxidase-activating proteinase-2 from hemolymph of Manduca sexta: A bacteria-inducible serine proteinase containing two clip domains
    • DOI 10.1074/jbc.M205743200
    • Jiang H,Wang Y, Yu XQ, Kanost MR (2003) Prophenoloxidase-activating proteinase-2 from hemolymph of Manduca sexta, A bacteria-inducible serine proteinase containing two clip domains. J Biol Chem 278: 3552-3561. (Pubitemid 36801078)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.6 , pp. 3552-3561
    • Jiang, H.1    Wang, Y.2    Yu, X.-Q.3    Kanost, M.R.4
  • 20
    • 0002728435 scopus 로고    scopus 로고
    • In vitro activation of pro-phenol-oxidase by two kinds of pro-phenol- oxidase-activating factors isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae
    • DOI 10.1046/j.1432-1327.1998.2540050.x
    • Lee SY, Kwon TH, Hyun JH, Choi JS, Kawabata SI, et al. (1998) In vitro activation of pro-phenol-oxidase by two kinds of pro-phenol-oxidase-activating factors isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae. FEBS 254: 50-57. (Pubitemid 28255067)
    • (1998) European Journal of Biochemistry , vol.254 , Issue.1 , pp. 50-57
    • Lee, S.Y.1    Kwon, T.H.2    Hyun, J.H.3    Choi, J.S.4    Kawabata, S.-I.5    Iwanaga, S.6    Lee, B.L.7
  • 21
    • 43149121130 scopus 로고    scopus 로고
    • A three-step proteolytic cascade mediates the activation of the peptidoglycan-induced toll pathway in an insect
    • Kim CH, Kim SJ, Kan H, Kwon HM, Roh KB, et al. (2008) A three-step proteolytic cascade mediates the activation of the peptidoglycan-induced toll pathway in an insect. J Biol Chem 283: 7599-7607.
    • (2008) J Biol Chem , vol.283 , pp. 7599-7607
    • Kim, C.H.1    Kim, S.J.2    Kan, H.3    Kwon, H.M.4    Roh, K.B.5
  • 22
    • 3543017971 scopus 로고    scopus 로고
    • Innate immunity in the malaria vector Anopheles gambiae: Comparative and functional genomics
    • DOI 10.1242/jeb.01066
    • Osta MA, Christophides GK, Vlachou D, Kafatos FC (2004) Innate immunity in the malaria vector Anopheles gambiae: comparative and functional genomics. J Exp Biol 207: 2551-2563. (Pubitemid 39009310)
    • (2004) Journal of Experimental Biology , vol.207 , Issue.15 , pp. 2551-2563
    • Osta, M.A.1    Christophides, G.K.2    Vlachou, D.3    Kafatos, F.C.4
  • 23
    • 19044375900 scopus 로고    scopus 로고
    • Mosquito immunity against Plasmodium
    • DOI 10.1016/j.ibmb.2005.02.009, PII S0965174805000640, Genetic Manipulations of Insects
    • Michel K, Kafatos FC (2005) Mosquito immunity against Plasmodium. Insect Biochem Mol Biol 35: 677-689. (Pubitemid 40707631)
    • (2005) Insect Biochemistry and Molecular Biology , vol.35 , Issue.7 , pp. 677-689
    • Michel, K.1    Kafatos, F.C.2
  • 24
    • 0037290892 scopus 로고    scopus 로고
    • Drosophila immunity: Paths and patterns
    • Hultmark D (2003) Drosophila immunity: paths and patterns. Curr Opin Immunol 15: 12-19.
    • (2003) Curr Opin Immunol , vol.15 , pp. 12-19
    • Hultmark, D.1
  • 25
    • 0033953792 scopus 로고    scopus 로고
    • The clip-domain family of serine proteinases in arthropods
    • DOI 10.1016/S0965-1748(99)00113-7, PII S0965174899001137
    • Jiang H, Kanost MR (2000) The clip-domain family of serine proteinases in arthropods. Insect Biochem Mol Biol 30: 95-105. (Pubitemid 30096721)
    • (2000) Insect Biochemistry and Molecular Biology , vol.30 , Issue.2 , pp. 95-105
    • Jiang, H.1    Kanost, M.R.2
  • 30
    • 36749066016 scopus 로고    scopus 로고
    • Comparative genomic analysis of the Tribolium immune system
    • Zou Z, Evans JD, Lu Z, Zhao P, Williams M, et al. (2007) Comparative genomic analysis of the Tribolium immune system. Genome Biol 8: R177.
    • (2007) Genome Biol , vol.8
    • Zou, Z.1    Evans, J.D.2    Lu, Z.3    Zhao, P.4    Williams, M.5
  • 31
    • 59649097832 scopus 로고    scopus 로고
    • A genome-wide analysis of genes and gene families involved in innate immunity of Bombyx mori
    • Tanaka H, Ishibashi J, Fujita K, Nakajima Y, Sagisaka A, et al. (2008) A genome-wide analysis of genes and gene families involved in innate immunity of Bombyx mori. Insect Biochem Mol Biol 38: 1087-1110.
    • (2008) Insect Biochem Mol Biol , vol.38 , pp. 1087-1110
    • Tanaka, H.1    Ishibashi, J.2    Fujita, K.3    Nakajima, Y.4    Sagisaka, A.5
  • 32
    • 50649122770 scopus 로고    scopus 로고
    • EagleView: A genome assembly viewer for next-generation sequencing technologies
    • Huang W, Marth G (2008) EagleView: a genome assembly viewer for next-generation sequencing technologies. Genome Res 18: 1538-1543.
    • (2008) Genome Res , vol.18 , pp. 1538-1543
    • Huang, W.1    Marth, G.2
  • 33
    • 79953685152 scopus 로고    scopus 로고
    • The impact of next-generation sequencing on genomics
    • Zhang J, Chiodini R, Badr A, Zhang G (2011) The impact of next-generation sequencing on genomics. J Genet Genomics 38: 95-109.
    • (2011) J Genet Genomics , vol.38 , pp. 95-109
    • Zhang, J.1    Chiodini, R.2    Badr, A.3    Zhang, G.4
  • 35
    • 84874716210 scopus 로고    scopus 로고
    • The genome- and transcriptome-wide analysis of innate immunity in the brown planthopper, Nilaparvata lugens
    • Bao YY, Qu LY, Zhao D, Chen LB, Jin HY, et al. (2013) The genome- and transcriptome-wide analysis of innate immunity in the brown planthopper, Nilaparvata lugens. BMC Genomics 14: 160.
    • (2013) BMC Genomics , vol.14 , pp. 160
    • Bao, Y.Y.1    Qu, L.Y.2    Zhao, D.3    Chen, L.B.4    Jin, H.Y.5
  • 36
    • 79958161502 scopus 로고    scopus 로고
    • A comprehensive transcriptome and immune-gene repertoire of the lepidopteran model host Galleria mellonella
    • Vogel H, Altincicek B, Glockner G, Vilcinskas A (2011) A comprehensive transcriptome and immune-gene repertoire of the lepidopteran model host Galleria mellonella. BMC Genomics 12: 308.
    • (2011) BMC Genomics , vol.12 , pp. 308
    • Vogel, H.1    Altincicek, B.2    Glockner, G.3    Vilcinskas, A.4
  • 37
    • 84879118552 scopus 로고    scopus 로고
    • Asian corn borer (ACB) and non-ACB pests in GM corn (Zea mays L.) in the Philippines
    • Afidchao MM, Musters C, de Snoo GR (2013) Asian corn borer (ACB) and non-ACB pests in GM corn (Zea mays L.) in the Philippines. Pest Manag Sci 69: 792-801.
    • (2013) Pest Manag Sci , vol.69 , pp. 792-801
    • Afidchao, M.M.1    Musters, C.2    De Snoo, G.R.3
  • 38
    • 0033856896 scopus 로고    scopus 로고
    • Colonization of corn, Zea mays, by the entomopathogenic fungus Beauveria bassiana
    • DOI 10.1128/AEM.66.8.3468-3473.2000
    • Wagner BL, Lewis LC (2000) Colonization of corn, Zea mays, by the entomopathogenic fungus Beauveria bassiana. Appl Environ Microbiol 66: 3468-3473. (Pubitemid 30624590)
    • (2000) Applied and Environmental Microbiology , vol.66 , Issue.8 , pp. 3468-3473
    • Wagner, B.L.1    Lewis, L.C.2
  • 39
    • 78650894318 scopus 로고    scopus 로고
    • The gene, expression pattern and subcellular localization of chitin synthase B from the insect Ostrinia furnacalis
    • Qu M, Liu T, Yang J, Yang Q (2011) The gene, expression pattern and subcellular localization of chitin synthase B from the insect Ostrinia furnacalis. Biochem Biophys Res Commun 404: 302-307.
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 302-307
    • Qu, M.1    Liu, T.2    Yang, J.3    Yang, Q.4
  • 40
  • 43
    • 0033290515 scopus 로고    scopus 로고
    • ESTScan: A program for detecting, evaluating, and reconstructing potential coding regions in EST sequences
    • Iseli C, Jongeneel CV, Bucher P (1999) ESTScan: a program for detecting, evaluating, and reconstructing potential coding regions in EST sequences. Proc Int Conf Intell Syst Mol Biol: 138-148.
    • (1999) Proc Int Conf Intell Syst Mol Biol , pp. 138-148
    • Iseli, C.1    Jongeneel, C.V.2    Bucher, P.3
  • 44
    • 24644503098 scopus 로고    scopus 로고
    • Blast2GO: A universal tool for annotation, visualization and analysis in functional genomics research
    • DOI 10.1093/bioinformatics/bti610
    • Conesa A, Gotz S, Garcia-Gomez JM, Terol J, Talon M, et al. (2005) Blast2GO: a universal tool for annotation, visualization and analysis in functional genomics research. Bioinformatics 21: 3674-3676. (Pubitemid 41264107)
    • (2005) Bioinformatics , vol.21 , Issue.18 , pp. 3674-3676
    • Conesa, A.1    Gotz, S.2    Garcia-Gomez, J.M.3    Terol, J.4    Talon, M.5    Robles, M.6
  • 46
    • 62349130698 scopus 로고    scopus 로고
    • Ultrafast and memory-efficient alignment of short DNA sequences to the human genome
    • Langmead B, Trapnell C, Pop M, Salzberg SL (2009) Ultrafast and memory-efficient alignment of short DNA sequences to the human genome. Genome Biol 10: R25.
    • (2009) Genome Biol , vol.10
    • Langmead, B.1    Trapnell, C.2    Pop, M.3    Salzberg, S.L.4
  • 47
    • 46249106990 scopus 로고    scopus 로고
    • Mapping and quantifying mammalian transcriptomes by RNA-Seq
    • DOI 10.1038/nmeth.1226, PII NMETH.1226
    • Mortazavi A, Williams BA, McCue K, Schaeffer L, Wold B (2008) Mapping and quantifying mammalian transcriptomes by RNA-Seq. Nat Methods 5: 621-628. (Pubitemid 351911867)
    • (2008) Nature Methods , vol.5 , Issue.7 , pp. 621-628
    • Mortazavi, A.1    Williams, B.A.2    McCue, K.3    Schaeffer, L.4    Wold, B.5
  • 48
    • 0030681260 scopus 로고    scopus 로고
    • The significance of digital gene expression profiles
    • Audic S, Claverie JM (1997) The significance of digital gene expression profiles. Genome Res 7: 986-995. (Pubitemid 27487763)
    • (1997) Genome Research , vol.7 , Issue.10 , pp. 986-995
    • Audic, S.1    Claverie, J.-M.2
  • 49
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini Y, Hochberg Y (1995) Controlling the false discovery rate: a practical and powerful approach to multiple testing. J Royal Stat Soci Series B: 289-300.
    • (1995) J Royal Stat Soci Series B , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 50
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, et al. (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28: 2731-2739.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5
  • 51
    • 0035710746 scopus 로고    scopus 로고
    • -DeltaDeltaCT method
    • DOI 10.1006/meth.2001.1262
    • Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2 (-Delta Delta C(T)) Method. Methods 25: 402-408. (Pubitemid 34164012)
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 52
    • 0033591428 scopus 로고    scopus 로고
    • Phylogenetic perspectives in innate immunity
    • DOI 10.1126/science.284.5418.1313
    • Hoffmann JA, Kafatos FC, Janeway CA, Ezekowitz RA (1999) Phylogenetic perspectives in innate immunity. Science 284: 1313-1318. (Pubitemid 29289650)
    • (1999) Science , vol.284 , Issue.5418 , pp. 1313-1318
    • Hoffmann, J.A.1    Kafatos, F.C.2    Janeway Jr., C.A.3    Ezekowitz, R.A.B.4
  • 53
    • 0029884417 scopus 로고    scopus 로고
    • Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori
    • DOI 10.1074/jbc.271.23.13854
    • Yoshida H, Kinoshita K, Ashida M (1996) Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori. J Biol Chem 271: 13854-13860. (Pubitemid 26185431)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.23 , pp. 13854-13860
    • Yoshida, H.1    Kinoshita, K.2    Ashida, M.3
  • 54
    • 77953139933 scopus 로고    scopus 로고
    • Involvement of Manduca sexta peptidoglycan recognition protein-1 in the recognition of bacteria and activation of prophenoloxidase system
    • Sumathipala N, Jiang H (2010) Involvement of Manduca sexta peptidoglycan recognition protein-1 in the recognition of bacteria and activation of prophenoloxidase system. Insect Biochem Mol Biol 40: 487-495.
    • (2010) Insect Biochem Mol Biol , vol.40 , pp. 487-495
    • Sumathipala, N.1    Jiang, H.2
  • 55
    • 84886099320 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins in Drosophila immunity
    • doi: 10.1016/j.dci.2013.06.006
    • Kurata S (2013) Peptidoglycan recognition proteins in Drosophila immunity. Dev Comp Immunol. doi: 10.1016/j.dci.2013.06.006.
    • (2013) Dev Comp Immunol
    • Kurata, S.1
  • 56
    • 0034610370 scopus 로고    scopus 로고
    • A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster
    • Werner T, Liu G, Kang D, Ekengren S, Steiner H, et al. (2000) A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster. Proc Natl Acad Sci U S A 97: 13772-13777.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 13772-13777
    • Werner, T.1    Liu, G.2    Kang, D.3    Ekengren, S.4    Steiner, H.5
  • 57
    • 0034693324 scopus 로고    scopus 로고
    • Gram-negative bacteria-binding protein, a pattern recognition receptor for lipopolysaccharide and beta-1, 3-glucan that mediates the signaling for the induction of innate immune genes in Drosophila melanogaster cells
    • Kim YS, Ryu JH, Han SJ, Choi KH, Nam KB, et al. (2000) Gram-negative bacteria-binding protein, a pattern recognition receptor for lipopolysaccharide and beta-1, 3-glucan that mediates the signaling for the induction of innate immune genes in Drosophila melanogaster cells. J Biol Chem 275: 32721-32727.
    • (2000) J Biol Chem , vol.275 , pp. 32721-32727
    • Kim, Y.S.1    Ryu, J.H.2    Han, S.J.3    Choi, K.H.4    Nam, K.B.5
  • 58
    • 0024297132 scopus 로고
    • Purification of a beta-1, 3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori
    • Ochiai M, Ashida M (1988) Purification of a beta-1, 3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori. J Biol Chem 263: 12056-12062.
    • (1988) J Biol Chem , vol.263 , pp. 12056-12062
    • Ochiai, M.1    Ashida, M.2
  • 59
    • 0034677596 scopus 로고    scopus 로고
    • A beta1,3-glucan recognition protein from an insect, Manduca sexta, agglutinates microorganisms and activates the phenoloxidase cascade
    • DOI 10.1074/jbc.275.11.7505
    • Ma C, Kanost MR (2000) A beta1, 3-glucan recognition protein from an insect, Manduca sexta, agglutinates microorganisms and activates the phenoloxidase cascade. J Biol Chem 275: 7505-7514. (Pubitemid 30159646)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.11 , pp. 7505-7514
    • Ma, C.1    Kanost, M.R.2
  • 60
    • 0742270922 scopus 로고    scopus 로고
    • Beta-1,3-Glucan recognition protein-2 (betaGRP-2) from Manduca sexta: An acute-phase protein that binds beta-1,3-glucan and lipoteichoic acid to aggregate fungi and bacteria and stimulate prophenoloxidase activation
    • DOI 10.1016/j.ibmb.2003.09.006
    • Jiang H, Ma C, Lu ZQ, Kanost MR (2004) Beta-1, 3-glucan recognition protein-2 (betaGRP-2)from Manduca sexta;an acute-phase protein that binds beta-1, 3-glucan and lipoteichoic acid to aggregate fungi and bacteria and stimulate prophenoloxidase activation. Insect Biochem Mol Biol 34: 89-100. (Pubitemid 38157615)
    • (2004) Insect Biochemistry and Molecular Biology , vol.34 , Issue.1 , pp. 89-100
    • Jiang, H.1    Ma, C.2    Lu, Z.-Q.3    Kanost, M.R.4
  • 61
    • 0034681346 scopus 로고    scopus 로고
    • A pattern-recognition protein for beta-1,3-glucan. The binding domain and the cDNA cloning of beta-1,3-glucan recognition protein from the silkworm, Bombyx mori
    • DOI 10.1074/jbc.275.7.4995
    • Ochiai M, Ashida M (2000) A pattern-recognition protein for beta-1, 3-glucan. The binding domain and the cDNA cloning of beta-1, 3-glucan recognition protein from the silkworm, Bombyx mori. J Biol Chem 275: 4995-5002. (Pubitemid 30108896)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.7 , pp. 4995-5002
    • Ochiai, M.1    Ashida, M.2
  • 62
    • 67650895881 scopus 로고    scopus 로고
    • Solution structure of the silkworm betaGRP/GNBP3 N-terminal domain reveals the mechanism for beta-1, 3-glucan-specific recognition
    • Takahasi K, Ochiai M, Horiuchi M, Kumeta H, Ogura K, et al. (2009) Solution structure of the silkworm betaGRP/GNBP3 N-terminal domain reveals the mechanism for beta-1, 3-glucan-specific recognition. Proc Natl Acad Sci U S A 106: 11679-11684.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 11679-11684
    • Takahasi, K.1    Ochiai, M.2    Horiuchi, M.3    Kumeta, H.4    Ogura, K.5
  • 63
    • 70350417515 scopus 로고    scopus 로고
    • The N-terminal domain of Drosophila Gram-negative binding protein 3 (GNBP3) defines a novel family of fungal pattern recognition receptors
    • Mishima Y, Quintin J, Aimanianda V, Kellenberger C, Coste F, et al. (2009) The N-terminal domain of Drosophila Gram-negative binding protein 3 (GNBP3) defines a novel family of fungal pattern recognition receptors. J Biol Chem 284: 28687-28697.
    • (2009) J Biol Chem , vol.284 , pp. 28687-28697
    • Mishima, Y.1    Quintin, J.2    Aimanianda, V.3    Kellenberger, C.4    Coste, F.5
  • 64
    • 2942617149 scopus 로고    scopus 로고
    • Immulectin-2, a pattern recognition receptor that stimulates hemocyte encapsulation and melanization in the tobacco hornworm, Manduca sexta
    • Yu XQ, Kanost MR (2004) Immulectin-2, a pattern recognition receptor that stimulates hemocyte encapsulation and melanization in the tobacco hornworm, Manduca sexta. Dev Comp Immunol 28: 891-900.
    • (2004) Dev Comp Immunol , vol.28 , pp. 891-900
    • Yu, X.Q.1    Kanost, M.R.2
  • 65
    • 0034535375 scopus 로고    scopus 로고
    • Immulectin-2, a lipopolysaccharide-specific lectin from an insect, Manduca sexta, is induced in response to gram-negative bacteria
    • Yu XQ, Kanost MR (2000) Immulectin-2, a lipopolysaccharide-specific lectin from an insect, Manduca sexta, is induced in response to gram-negative bacteria. J Biol Chem 275: 37373-37381.
    • (2000) J Biol Chem , vol.275 , pp. 37373-37381
    • Yu, X.Q.1    Kanost, M.R.2
  • 66
    • 0032993577 scopus 로고    scopus 로고
    • The lipopolysaccharide-binding protein participating in hemocyte nodule formation in the silkworm Bombyx mori is a novel member of the C-type lectin superfamily with two different tandem carbohydrate-recognition domains
    • DOI 10.1016/S0014-5793(98)01701-3, PII S0014579398017013
    • Koizumi N, Imamura M, Kadotani T, Yaoi K, Iwahana H, et al. (1999) The lipopolysaccharide- binding protein participating in hemocyte nodule formation in the silkworm Bombyx mori is a novel member of the C-type lectin superfamily with two different tandem carbohydrate-recognition domains. FEBS Lett 443: 139-143. (Pubitemid 29078619)
    • (1999) FEBS Letters , vol.443 , Issue.2 , pp. 139-143
    • Koizumi, N.1    Imamura, M.2    Kadotani, T.3    Yaoi, K.4    Iwahana, H.5    Sato, R.6
  • 67
    • 0037364965 scopus 로고    scopus 로고
    • Manduca sexta lipopolysaccharide-specific immulectin-2 protects larvae from bacterial infection
    • Yu XQ, Kanost MR (2003) Manduca sexta lipopolysaccharide-specific immulectin-2 protects larvae from bacterial infection. Dev Comp Immunol 27: 189-196.
    • (2003) Dev Comp Immunol , vol.27 , pp. 189-196
    • Yu, X.Q.1    Kanost, M.R.2
  • 68
    • 0033959641 scopus 로고    scopus 로고
    • Two carbohydrate recognition domains of Hyphantria cunea lectin bind to bacterial lipopolysaccharides through O-specific chain
    • DOI 10.1016/S0014-5793(00)01127-3, PII S0014579300011273
    • Shin SW, Park DS, Kim SC, Park HY (2000) Two carbohydrate recognition domains of Hyphantria cunea lectin bind to bacterial lipopolysaccharides through O-specific chain. FEBS Lett 467: 70-74. (Pubitemid 30069545)
    • (2000) FEBS Letters , vol.467 , Issue.1 , pp. 70-74
    • Shin, S.W.1    Park, D.-S.2    Kim, S.C.3    Park, H.-Y.4
  • 69
    • 0031036860 scopus 로고    scopus 로고
    • The role of selectins in Drosophila eye and bristle development
    • Leshko-Lindsay LA, Corces VG (1997) The role of selectins in Drosophila eye and bristle development. Development 124: 169-180.
    • (1997) Development , vol.124 , pp. 169-180
    • Leshko-Lindsay, L.A.1    Corces, V.G.2
  • 71
    • 33750477010 scopus 로고    scopus 로고
    • Comparative analysis of serine protease-related genes in the honey bee genome: Possible involvement in embryonic development and innate immunity
    • DOI 10.1111/j.1365-2583.2006.00684.x
    • Zou Z, Lopez DL, Kanost MR, Evans JD, Jiang H (2006) Comparative analysis of serine protease-related genes in the honey bee genome: possible involvement in embryonic development and innate immunity. Insect Mol Biol 15: 603-614. (Pubitemid 44652090)
    • (2006) Insect Molecular Biology , vol.15 , Issue.5 , pp. 603-614
    • Zou, Z.1    Lopez, D.L.2    Kanost, M.R.3    Evans, J.D.4    Jiang, H.5
  • 73
    • 0037311545 scopus 로고    scopus 로고
    • Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm, Manduca sexta
    • DOI 10.1016/S0965-1748(02)00191-1
    • Yu XQ, Jiang H, Wang Y, Kanost MR (2003) Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm, Manduca sexta. Insect Biochem Mol Biol 33: 197-208. (Pubitemid 36154283)
    • (2003) Insect Biochemistry and Molecular Biology , vol.33 , Issue.2 , pp. 197-208
    • Yu, X.-Q.1    Jiang, H.2    Wang, Y.3    Kanost, M.R.4
  • 74
    • 54449085542 scopus 로고    scopus 로고
    • Molecular control of phenoloxidase- induced melanin synthesis in an insect
    • Kan H, Kim CH, Kwon HM, Park JW, Roh KB, et al. (2008) Molecular control of phenoloxidase- induced melanin synthesis in an insect. J Biol Chem 283: 25316-25323.
    • (2008) J Biol Chem , vol.283 , pp. 25316-25323
    • Kan, H.1    Kim, C.H.2    Kwon, H.M.3    Park, J.W.4    Roh, K.B.5
  • 75
    • 0037472685 scopus 로고    scopus 로고
    • Serine proteases and their homologs in the Drosophila melanogaster genome: An initial analysis of sequence conservation and phylogenetic relationships
    • DOI 10.1016/S0378-1119(02)01187-3
    • Ross J, Jiang H, Kanost MR, Wang Y (2003) Serine proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships. Gene 304: 117-131. (Pubitemid 36140137)
    • (2003) Gene , vol.304 , Issue.1-2 , pp. 117-131
    • Ross, J.1    Jiang, H.2    Kanost, M.R.3    Wang, Y.4
  • 76
    • 40549103093 scopus 로고    scopus 로고
    • CLIP-domain serine proteases in Drosophila innate immunity
    • Jang IH, Nam HJ, Lee WJ (2008) CLIP-domain serine proteases in Drosophila innate immunity. BMB reports 41: 102-107.
    • (2008) BMB Reports , vol.41 , pp. 102-107
    • Jang, I.H.1    Nam, H.J.2    Lee, W.J.3
  • 77
    • 61849184076 scopus 로고    scopus 로고
    • A comparative analysis of serpin genes in the silkworm genome
    • Zou Z, Picheng Z, Weng H, Mita K, Jiang H (2009) A comparative analysis of serpin genes in the silkworm genome. Genomics 93: 367-375.
    • (2009) Genomics , vol.93 , pp. 367-375
    • Zou, Z.1    Picheng, Z.2    Weng, H.3    Mita, K.4    Jiang, H.5
  • 78
    • 4544337752 scopus 로고    scopus 로고
    • A pattern recognition serine proteinase triggers the prophenoloxidase activation cascade in the tobacco hornworm, Manduca sexta
    • DOI 10.1074/jbc.M404584200
    • Ji C, Wang Y, Guo X, Hartson S, Jiang H (2004) A pattern recognition serine proteinase triggers the prophenoloxidase activation cascade in the tobacco hornworm, Manduca sexta. J Biol Chem 279: 34101-34106. (Pubitemid 39318031)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34101-34106
    • Ji, C.1    Wang, Y.2    Guo, X.3    Hartson, S.4    Jiang, H.5
  • 79
    • 0032992544 scopus 로고    scopus 로고
    • Serine proteinase inhibitors in arthropod immunity
    • Kanost MR (1999) Serine proteinase inhibitors in arthropod immunity. Dev Comp Immunol 23: 291-301.
    • (1999) Dev Comp Immunol , vol.23 , pp. 291-301
    • Kanost, M.R.1
  • 80
    • 77955302605 scopus 로고    scopus 로고
    • Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems
    • Silverman GA, Whisstock JC, Bottomley SP, Huntington JA, Kaiserman D, et al. (2010) Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems. J Biol Chem 285: 24299-24305.
    • (2010) J Biol Chem , vol.285 , pp. 24299-24305
    • Silverman, G.A.1    Whisstock, J.C.2    Bottomley, S.P.3    Huntington, J.A.4    Kaiserman, D.5
  • 81
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins PG (2002) Serpin structure, mechanism, and function. Chem Rev 102: 4751-4803.
    • (2002) Chem Rev , vol.102 , pp. 4751-4803
    • Gettins, P.G.1
  • 82
    • 28044443956 scopus 로고    scopus 로고
    • Anopheles gambiae SRPN2 facilitates midgut invasion by the malaria parasite Plasmodium berghei
    • DOI 10.1038/sj.embor.7400478, PII 7400478
    • Michel K, Budd A, Pinto S, Gibson TJ, Kafatos FC (2005) Anopheles gambiae SRPN2 facilitates midgut invasion by the malaria parasite Plasmodium berghei. EMBO reports 6: 891-897. (Pubitemid 43108682)
    • (2005) EMBO Reports , vol.6 , Issue.9 , pp. 891-897
    • Michel, K.1    Budd, A.2    Pinto, S.3    Gibson, T.J.4    Kafatos, F.C.5
  • 83
    • 79958184410 scopus 로고    scopus 로고
    • Characterization of a regulatory unit that controls melanization and affects longevity of mosquitoes
    • An C, Budd A, Kanost MR, Michel K (2011) Characterization of a regulatory unit that controls melanization and affects longevity of mosquitoes. Cell Mol Life Sci 68: 1929-1939.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 1929-1939
    • An, C.1    Budd, A.2    Kanost, M.R.3    Michel, K.4
  • 86
    • 0344875577 scopus 로고    scopus 로고
    • Manduca sexta Serpin-3 Regulates Prophenoloxidase Activation in Response to Infection by Inhibiting Prophenoloxidase-activating Proteinases
    • DOI 10.1074/jbc.M309682200
    • Zhu Y, Wang Y, Gorman MJ, Jiang H, KanostMR (2003) Manduca sexta serpin-3 regulates prophenoloxidase activation in response to infection by inhibiting prophenoloxidase-activating proteinases. J Biol Chem 278: 46556-46564. (Pubitemid 37452229)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 46556-46564
    • Zhu, Y.1    Wang, Y.2    Gorman, M.J.3    Jiang, H.4    Kanost, M.R.5
  • 87
    • 17644379634 scopus 로고    scopus 로고
    • Identification of plasma proteases inhibited by Manduca sexta serpin-4 and serpin-5 and their association with components of the prophenol oxidase activation pathway
    • DOI 10.1074/jbc.M500532200
    • Tong Y, Jiang H, Kanost MR (2005) Identification of plasma proteases inhibited by Manduca sexta serpin-4 and serpin-5 and their association with components of the prophenol oxidase activation pathway. J Biol Chem 280: 14932-14942. (Pubitemid 40562844)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 14932-14942
    • Tong, Y.1    Jiang, H.2    Kanost, M.R.3
  • 88
    • 72149095466 scopus 로고    scopus 로고
    • Three pairs of protease-serpin complexes cooperatively regulate the insect innate immune responses
    • Jiang R, Kim EH, Gong JH, Kwon HM, Kim CH, et al. (2009) Three pairs of protease-serpin complexes cooperatively regulate the insect innate immune responses. J Biol Chem 284: 35652-35658.
    • (2009) J Biol Chem , vol.284 , pp. 35652-35658
    • Jiang, R.1    Kim, E.H.2    Gong, J.H.3    Kwon, H.M.4    Kim, C.H.5
  • 90
    • 34447648523 scopus 로고    scopus 로고
    • Proteolytic activation of pro-spatzle is required for the induced transcription of antimicrobial peptide genes in lepidopteran insects
    • DOI 10.1016/j.dci.2007.01.001, PII S0145305X07000122
    • Wang Y, Cheng T, Rayaprolu S, Zou Z, Xia Q, et al. (2007) Proteolytic activation of pro-spatzle is required for the induced transcription of antimicrobial peptide genes in lepidopteran insects. Dev Comp Immunol 31: 1002-1012. (Pubitemid 47095006)
    • (2007) Developmental and Comparative Immunology , vol.31 , Issue.10 , pp. 1002-1012
    • Wang, Y.1    Cheng, T.2    Rayaprolu, S.3    Zou, Z.4    Xia, Q.5    Xiang, Z.6    Jiang, H.7
  • 91
    • 73649085875 scopus 로고    scopus 로고
    • Proteolytic activation and function of the cytokine Spatzle in the innate immune response of a lepidopteran insect, Manduca sexta
    • An C, Jiang H, Kanost MR (2010) Proteolytic activation and function of the cytokine Spatzle in the innate immune response of a lepidopteran insect, Manduca sexta. FEBS J 277: 148-162.
    • (2010) FEBS J , vol.277 , pp. 148-162
    • An, C.1    Jiang, H.2    Kanost, M.R.3
  • 92
    • 0032033030 scopus 로고    scopus 로고
    • Proteolytic processing of the Drosophila Spatzle protein by Easter generates a dimeric NGF-like molecule with ventralising activity
    • DOI 10.1016/S0925-4773(98)00024-0, PII S0925477398000240
    • DeLotto Y, DeLotto R (1998) Proteolytic processing of the Drosophila Spatzle protein by easter generates a dimeric NGF-like molecule with ventralising activity. Mech Dev 72: 141-148. (Pubitemid 28186713)
    • (1998) Mechanisms of Development , vol.72 , Issue.1-2 , pp. 141-148
    • DeLotto, Y.1    DeLotto, R.2
  • 93
    • 0035856990 scopus 로고    scopus 로고
    • Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein
    • DOI 10.1038/414756a
    • Michel T, Reichhart JM, Hoffmann JA, Royet J (2001) Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein. Nature 414: 756-759. (Pubitemid 34000773)
    • (2001) Nature , vol.414 , Issue.6865 , pp. 756-759
    • Michel, T.1    Relchhart, J.2    Hoffmann, J.A.3    Royet, J.4
  • 95
    • 0034597766 scopus 로고    scopus 로고
    • Structural basis for signal transduction by the Toll/interleukin-1 receptor domains
    • Xu Y, Tao X, Shen B, Horng T, Medzhitov R, et al. (2000) Structural basis for signal transduction by the Toll/interleukin-1 receptor domains. Nature 408: 111-115.
    • (2000) Nature , vol.408 , pp. 111-115
    • Xu, Y.1    Tao, X.2    Shen, B.3    Horng, T.4    Medzhitov, R.5
  • 97
    • 33646356449 scopus 로고    scopus 로고
    • Pathogen recognition and signalling in the Drosophila innate immune response
    • Wang L, Ligoxygakis P (2006) Pathogen recognition and signalling in the Drosophila innate immune response. Immunobiology 211: 251-261.
    • (2006) Immunobiology , vol.211 , pp. 251-261
    • Wang, L.1    Ligoxygakis, P.2
  • 98
    • 0036167107 scopus 로고    scopus 로고
    • Drosophila innate immunity: An evolutionary perspective
    • DOI 10.1038/ni0202-121
    • Hoffmann JA, Reichhart JM (2002) Drosophila innate immunity: an evolutionary perspective. Nat Immunol 3: 121-126. (Pubitemid 34141441)
    • (2002) Nature Immunology , vol.3 , Issue.2 , pp. 121-126
    • Hoffmann, J.A.1    Reichhart, J.-M.2
  • 100
    • 0029162812 scopus 로고
    • Molecular cloning of insect pro-phenol oxidase: A copper-containing protein homologous to arthropod hemocyanin
    • Kawabata T, Yasuhara Y, Ochiai M, Matsuura S, Ashida M (1995) Molecular cloning of insect pro-phenol oxidase: a copper-containing protein homologous to arthropod hemocyanin. Proc Natl Acad Sci U S A 92: 7774-7778.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 7774-7778
    • Kawabata, T.1    Yasuhara, Y.2    Ochiai, M.3    Matsuura, S.4    Ashida, M.5
  • 101
    • 3242719716 scopus 로고    scopus 로고
    • Prophenoloxidase (proPO) activation in Manduca sexta: An analysis of molecular interactions among proPO, proPO-activating proteinase-3, and a cofactor
    • DOI 10.1016/j.ibmb.2004.03.008, PII S0965174804000487
    • Wang Y, Jiang H (2004) Prophenoloxidase (proPO) activation in Manduca sexta: an analysis of molecular interactions among proPO, proPO-activating proteinase-3, and a cofactor. Insect Biochem Mol Biol 34: 731-742. (Pubitemid 38946540)
    • (2004) Insect Biochemistry and Molecular Biology , vol.34 , Issue.8 , pp. 731-742
    • Wang, Y.1    Jiang, H.2
  • 102
    • 50049098836 scopus 로고    scopus 로고
    • Purification and characterization of hemolymph prophenoloxidase from Ostrinia furnacalis (Lepidoptera: Pyralidae) larvae
    • Feng C, Song Q, Lü W, Lu J (2008) Purification and characterization of hemolymph prophenoloxidase from Ostrinia furnacalis (Lepidoptera: Pyralidae) larvae. Comp Biochem Physiol B Biochem Mol Biol 151: 139-146.
    • (2008) Comp Biochem Physiol B Biochem Mol Biol , vol.151 , pp. 139-146
    • Feng, C.1    Song, Q.2    Lü, W.3    Lu, J.4
  • 103
    • 0029011721 scopus 로고
    • Reexamination of properties of prophenoloxidase isolated from larval hemolymph of the silkworm Bombyx mori
    • Yasuhara Y, Koizumi Y, Katagiri C, Ashida M (1995) Reexamination of properties of prophenoloxidase isolated from larval hemolymph of the silkworm Bombyx mori. Arch Biochem Biophys 320: 14-23.
    • (1995) Arch Biochem Biophys , vol.320 , pp. 14-23
    • Yasuhara, Y.1    Koizumi, Y.2    Katagiri, C.3    Ashida, M.4
  • 104
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • Andreu D, Rivas L (1998) Animal antimicrobial peptides: an overview. Biopolymers 47: 415-433.
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 105
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3: 238-250.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 107
    • 44749083112 scopus 로고    scopus 로고
    • Molecular characterization, phylogeny, and expression of c-type and g-type lysozymes in brill (Scophthalmus rhombus)
    • Jimenez-Cantizano RM, Infante C, Martin-Antonio B, Ponce M, Hachero I, et al. (2008) Molecular characterization, phylogeny, and expression of c-type and g-type lysozymes in brill (Scophthalmus rhombus). Fish Shellfish Immunol 25: 57-65.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 57-65
    • Jimenez-Cantizano, R.M.1    Infante, C.2    Martin-Antonio, B.3    Ponce, M.4    Hachero, I.5
  • 108
    • 34249791781 scopus 로고    scopus 로고
    • Immune upregulation of novel antibacterial proteins from silkmoths (Lepidoptera) that resemble lysozymes but lack muramidase activity
    • DOI 10.1016/j.ibmb.2007.03.013, PII S0965174807000677
    • Gandhe AS, Janardhan G, Nagaraju J (2007) Immune upregulation of novel antibacterial proteins from silkmoths (Lepidoptera) that resemble lysozymes but lack muramidase activity. Insect Biochem Mol Biol 37: 655-666. (Pubitemid 46844882)
    • (2007) Insect Biochemistry and Molecular Biology , vol.37 , Issue.7 , pp. 655-666
    • Gandhe, A.S.1    Janardhan, G.2    Nagaraju, J.3
  • 109
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • DOI 10.1038/292246a0
    • Steiner H, Hultmark D, Engstrom A, Bennich H, Boman HG (1981) Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292: 246-248. (Pubitemid 11001840)
    • (1981) Nature , vol.292 , Issue.5820 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3
  • 110
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: From invertebrates to vertebrates
    • DOI 10.1111/j.0105-2896.2004.0124.x
    • Bulet P, Stocklin R, Menin L (2004) Anti-microbial peptides: from invertebrates to vertebrates. Immunol Rev 198: 169-184. (Pubitemid 38406943)
    • (2004) Immunological Reviews , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 111
    • 0034050669 scopus 로고    scopus 로고
    • Review: Free radicals, antioxidants, and the immune system
    • Knight JA (2000) Review: Free radicals, antioxidants, and the immune system. Ann Clin Lab Sci 30: 145-158.
    • (2000) Ann Clin Lab Sci , vol.30 , pp. 145-158
    • Knight, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.